Literature summary for 1.4.99.6 extracted from

Yuan, H.; Xin, Y.; Hamelberg, D.; Gadda, G.
Insights on the mechanism of amine oxidation catalyzed by D-arginine dehydrogenase through pH and kinetic isotope effects (2011), J. Am. Chem. Soc., 133, 18957-18965.

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Organism

Organism	UniProt	Comment	Textmining
Pseudomonas aeruginosa	Q9HXE3	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-leucine + phenazine methosulfate	enzyme preferentially binds the zwitterionic form of the substrate. Isomerization of the Michaelis complex yields an enzyme-substrate complex competent for flavin reduction. Amine deprotonation triggers the oxidation reaction, with cleavage of the substrate NH and CH bonds occurring in an asynchronous fashion. Tyr53, on a mobile loop covering the active site, may participate in substrate binding and facilitate flavin reduction	Pseudomonas aeruginosa	? + NH3 + reduced phenazine methosulfate	-	?

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Release 2023.1 (January 2023)